Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex

Katsuhiko S. Murakami, Shoko Masuda, Elizabeth A. Campbell, Oriana Muzzin, Seth A. Darst

Research output: Contribution to journalArticle

504 Scopus citations

Abstract

The crystal structure of Thermus aquaticus RNA polymerase holoenzyme (α2ββ′ωσA) complexed with a fork-junction promoter DNA fragment has been determined by fitting high-resolution x-ray structures of individual components into a 6.5-angstrom resolution map. The DNA lies across one face of the holoenzyme, completely outside the RNA polymerase active site channel All sequence-specific contacts with core promoter elements are mediated by the subunit. A universally conserved tryptophan is ideally positioned to stack on the exposed face of the base pair at the upstream edge of the transcription bubble. Universally conserved basic residues of the or subunit provide critical contacts with the DNA phosphate backbone and play a role in directing the melted DNA template strand into the RNA polymerase active site. The structure explains how holoenzyme recognizes promoters containing variably spaced-10 and -35 elements and provides the basis for models of the closed and open promoter complexes.

Original languageEnglish (US)
Pages (from-to)1285-1290
Number of pages6
JournalScience
Volume296
Issue number5571
DOIs
StatePublished - May 17 2002

All Science Journal Classification (ASJC) codes

  • General

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